BMRB Entry 5318
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5318
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Title: Backbone and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain PubMed: 8181064
Deposition date: 2002-03-13 Original release date: 2002-05-01
Authors: Forman-Kay, Julie
Citation: Pascal, Steve; Gish, Gerry; Yamazaki, Toshio; Singer, Alex; Shoelson, Steven; Pawson, Tony; Kay, Lewis; Forman-Kay, Julie. "Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide" Cell 77, 461-472 (1994).
Assembly members:
PLCC SH2, polymer, 105 residues, Formula weight is not available
Natural source: Common Name: Cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PLCC SH2: GSPGIHESKEWYHASLTRAQ
AEHMLMRVPRDGAFLVRKRN
EPNSYAISFRAEGKIKHCRV
QQEGQTVMLGNSEFDSLVDL
ISYYEKHPLYRKMKLRYPIN
EENSS
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 98 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PLCC SH2 domain | 1 |
Entities:
Entity 1, PLCC SH2 domain 105 residues - Formula weight is not available
| 1 | GLY | SER | PRO | GLY | ILE | HIS | GLU | SER | LYS | GLU | ||||
| 2 | TRP | TYR | HIS | ALA | SER | LEU | THR | ARG | ALA | GLN | ||||
| 3 | ALA | GLU | HIS | MET | LEU | MET | ARG | VAL | PRO | ARG | ||||
| 4 | ASP | GLY | ALA | PHE | LEU | VAL | ARG | LYS | ARG | ASN | ||||
| 5 | GLU | PRO | ASN | SER | TYR | ALA | ILE | SER | PHE | ARG | ||||
| 6 | ALA | GLU | GLY | LYS | ILE | LYS | HIS | CYS | ARG | VAL | ||||
| 7 | GLN | GLN | GLU | GLY | GLN | THR | VAL | MET | LEU | GLY | ||||
| 8 | ASN | SER | GLU | PHE | ASP | SER | LEU | VAL | ASP | LEU | ||||
| 9 | ILE | SER | TYR | TYR | GLU | LYS | HIS | PRO | LEU | TYR | ||||
| 10 | ARG | LYS | MET | LYS | LEU | ARG | TYR | PRO | ILE | ASN | ||||
| 11 | GLU | GLU | ASN | SER | SER |
Samples:
sample_1: PLCC SH2, [U-99% 15N], 1.5 mM; sodium phosphate 100 mM
condition_1: pH: 6.4; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C- or 15N-edited NOESY-HSQC | sample_1 | not available | condition_1 |
| 3D 15N-edited TOCSY-HSQC | sample_1 | not available | condition_1 |
| CN NOESY-HSQC | sample_1 | not available | condition_1 |
| HBCBCA(CO)NNH | sample_1 | not available | condition_1 |
| HNCACB | sample_1 | not available | condition_1 |
| (HB)CB(CGCD)HD | sample_1 | not available | condition_1 |
| (HB)CB(CGCDCE)HE | sample_1 | not available | condition_1 |
| HMQC J | sample_1 | not available | condition_1 |
Software:
X-PLOR - combined distance geometry-simulated annealing calculations
STEREOSEARCH - extraction of torsion angle restraint values
NMR spectrometers:
- Varian UNITY 500 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
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